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1 SHIP-1 (Src homology [SH2] domain-containing inositol phosphatase).
2 e SopE-dependent activation of an endogenous inositol phosphatase.
3 vity, thus implicating the involvement of an inositol phosphatase.
4 2) domain-containing cytoplasmic tyrosine or inositol phosphatases.
5 (SHP) 2 and Src homology domain 2-containing inositol phosphatase 1 (SHIP-1) and internalization of I
6  EAT-2 was mediated by SH2 domain-containing inositol phosphatase 1 (SHIP-1), which was recruited via
7                           The SH2-containing inositol phosphatase-1 (SHIP-1) is a 5' inositol phospha
8                        SH2 domain-containing inositol phosphatase-1 (SHIP-1) is phosphorylated on Y10
9 SHIP1 to be phosphorylated and stimulate its inositol phosphatase activity.
10 ding evidence that Src homology 2 containing inositol phosphatase, an inhibitor of NF-kappaB activati
11 kines and the upregulation of SH2-containing inositol phosphatase, an inhibitor of NF-kappaB signalin
12  and expression of Src homology 2-containing inositol phosphatase and Src homology 2-containing prote
13 ember function: first, several targets of an inositol-phosphatase-dependent inhibitory signaling path
14 ortance of the tyrosine phosphatases and the inositol phosphatase differs depending on the cell type.
15 int mutations of the signature motifs in the inositol phosphatase domain abolish SHIP's ability to in
16 atic mutagenesis approach, we identified the inositol phosphatase domain of SHIP between amino acids
17 is novel protein, p150(ship) (SH2-containing inositol phosphatase), identifies a component of a new g
18 nositol phosphatase) or SHIP (SH2-containing inositol phosphatase) is a recently identified SH2 domai
19 ning inositol phosphatase-1 (SHIP-1) is a 5' inositol phosphatase known to negatively regulate the pr
20                                SHIP1 is a 5'-inositol phosphatase known to negatively regulate the si
21                                  SHIP2, a 5'-inositol phosphatase, localizes at the invadopodium core
22 usly identified as Src homology 2-containing inositol phosphatase, only under conditions of negative
23                               SIP (signaling inositol phosphatase) or SHIP (SH2-containing inositol p
24                                          The inositol phosphatases phosphatase and tensin homologue (
25 me 10 or src homology 2 domain-containing 5' inositol phosphatase, phosphatases that negatively regul
26 the Dictyostelium genome called phospholipid-inositol phosphatase (PLIP), which defines a new subfami
27 ase (pBtk) and phosphorylated SH2-containing inositol phosphatase (pSHIP), are reduced and enhanced,
28 y, experiments identify up-regulation of the inositol phosphatase PTEN (phosphatase and tensin homolo
29 mmatory signaling by direct targeting of the inositol phosphatase PTEN, the signaling inhibitor SOCS1
30 CD19, as well as increased expression of the inositol phosphatase PTEN.
31 le signaling enzymes and is regulated by the inositol phosphatases PTEN (phosphatase and tensin homol
32 nts of protein-tyrosine phosphatase-like myo-inositol phosphatases (PTPLPs) from the non-pathogenic b
33         Disruption of the negative signaling inositol phosphatase, SH2-containing inositol-5-phosphat
34                                          The inositol phosphatase SHIP binds to the FcgammaRIIB1 rece
35                                          The inositol phosphatase SHIP has been implicated in signali
36                SHP-1 and -2 and the novel 5'-inositol phosphatase SHIP have recently been shown to fu
37                              Activity of the inositol phosphatase SHIP is required for this negative
38 B cells results in the recruitment of the 5'-inositol phosphatase SHIP to the signaling complex.
39  resulted in enhanced phosphorylation of the inositol phosphatase SHIP, association of SHIP with Shc,
40 lving the tyrosine phosphatase SHP-1 and the inositol phosphatase SHIP-1 are required to maintain ane
41                                 Although the inositol phosphatase SHIP-1 is generally thought to inhi
42 y Fc gamma RIIa is tightly controlled by the inositol phosphatase SHIP-1, and the protein-tyrosine ph
43  cells by the expression and function of the inositol phosphatase SHIP-2.
44 tivation, and its intracellular effector the inositol phosphatase SHIP.
45 ein tyrosine phosphatase SHP-1 and SHP-2 and inositol phosphatase SHIP.
46 gate MPN-like disease in animals lacking the inositol phosphatase SHIP.
47 tion mediated by Fc gamma RIIb1 requires the inositol phosphatase SHIP.
48 ly identified as an SH2 domain containing 5'-inositol phosphatase (SHIP) and has been implicated in t
49 uggest that the receptor uses SH2-containing inositol phosphatase (SHIP) and SH2-containing phosphoty
50  current study, the effect of SH2-containing inositol phosphatase (SHIP) expression on these biologic
51                  We find that SH2-containing inositol phosphatase (SHIP) influences the repertoire of
52                               SH2-containing Inositol Phosphatase (SHIP) is a 145 kD protein expresse
53 ough the Src homology 2 domain-containing 5' inositol phosphatase (SHIP) is a well-known mediator of
54 atase Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP) is phosphorylated and associ
55 de, we have found that the SH2-containing 5'-inositol phosphatase (SHIP) is phosphorylated on tyrosin
56  (PTEN) and Src homology 2 domain-containing inositol phosphatase (SHIP) negatively regulate phosphat
57 h IL-4R alpha signals Shc and SH2-containing inositol phosphatase (SHIP) phosphorylation, we could no
58 a the Src homology region 2 (SH2)-containing inositol phosphatase (SHIP) SH2 domain.
59 is pathway is blocked when an SH2-containing inositol phosphatase (SHIP)-dependent inhibitory recepto
60 rformed by the 145-kDa SH2 domain-containing inositol phosphatase (SHIP).
61  (PTEN) and Src homology 2 domain-containing inositol phosphatase (SHIP-1), which hydrolyze PI(3,4,5)
62  tyrosine phosphorylation or activity of the inositol phosphatase, SHIP, in Lyn(-/-) BMMCs.
63 and the binding of the SH2 domain-containing inositol phosphatase, SHIP, to Fc gamma RIIB1.
64 bition is mediated by the recruitment of the inositol phosphatase, SHIP, to the Fc gammaRIIB1 phospho
65 reduction of tyrosine phosphorylation of the inositol phosphatase, SHIP.
66 d, in part, via diminished expression of the inositol phosphatase SHIP1 and increased activation of E
67  is associated with phosphorylation of the 5-inositol phosphatase SHIP1 and requires SHIP1 expression
68                The Src homology 2-containing inositol phosphatase SHIP1 functions in hemopoietic cell
69  in part via miR-155's direct effects on the inositol phosphatase SHIP1.
70              Mena also interacts with the 5' inositol phosphatase SHIP2, which is important for the r
71                      SH2 domain-containing 5-inositol phosphatase (SHIP2) is implicated in the develo
72       Here we investigate the role of the 5'-inositol phosphatase, SHIP2, and reveal an unexpected sc
73         Our recent studies revealed that the inositol phosphatase Src homology 2 (SH2) domain-contain
74 atase and tensin homolog), or SH2-containing inositol phosphatase suppressed the Btk(lo) phenotype in
75                          In contrast, the 5'-inositol phosphatase synaptojanin 1 localizes to CCPs an
76                                   SHIP is an inositol phosphatase that can reverse the activation eve
77                                SHIP1 is a 5' inositol phosphatase that dephosphorylates the phosphati
78                                   SHIP is an inositol phosphatase that downregulates PI3K-mediated ac
79                                Among several inositol phosphatases that regulate the availability of
80  such as Fc epsilon RI, recruit tyrosine and inositol phosphatases that results in diminished calcium
81                           The recruitment of inositol phosphatases to endocytic membranes mediates de
82 ing hemITAM can also couple to intracellular inositol phosphatases to modulate selected functional re
83 as SKIP (skeletal muscle and kidney enriched inositol phosphatase), which is highly expressed in the
84 t study we have demonstrated that SHIP-2, an inositol phosphatase with high-level homology to SHIP-1,

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